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Q63HQ0

- AP1AR_HUMAN

UniProt

Q63HQ0 - AP1AR_HUMAN

Protein

AP-1 complex-associated regulatory protein

Gene

AP1AR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      Previous versions | rss
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    Functioni

    Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-adaptin attenuates the release of the AP-1 complex from membranes. Regulates endosomal membrane traffic via association with AP-1 and KIF5B thus linking kinesin-based plus-end-directed microtubular transport to AP-1-dependent membrane traffic. May act as effector of AP-1 in calcium-induced endo-lysosome secretion. Inhibits Arp2/3 complex function; negatively regulates cell spreading, size and motility via intracellular sequestration of the Arp2/3 complex.4 Publications

    GO - Molecular functioni

    1. AP-1 adaptor complex binding Source: UniProtKB
    2. kinesin binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein localization Source: Ensembl
    2. negative regulation of cell motility Source: Ensembl
    3. negative regulation of receptor recycling Source: UniProtKB
    4. negative regulation of substrate adhesion-dependent cell spreading Source: MGI
    5. protein transport Source: UniProtKB-KW
    6. regulation of Arp2/3 complex-mediated actin nucleation Source: Ensembl
    7. vesicle targeting, trans-Golgi to endosome Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-1 complex-associated regulatory protein
    Alternative name(s):
    2c18
    Adaptor-related protein complex 1-associated regulatory protein
    Gamma-1-adaptin brefeldin A resistance protein
    Short name:
    GBAR
    Short name:
    Gamma-BAR
    Gamma-A1-adaptin and kinesin interactor
    Short name:
    Gadkin
    Gene namesi
    Name:AP1AR
    Synonyms:C4orf16
    ORF Names:PRO0971
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:28808. AP1AR.

    Subcellular locationi

    Golgi apparatustrans-Golgi network. Late endosome. Early endosome
    Note: Localizes to the juxta-nuclear Golgi region and to tubular structures throughout the cytoplasm, which are highly mobile and cycle between the juxta-nuclear area and the cell periphery.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. early endosome Source: UniProtKB-SubCell
    3. Golgi apparatus Source: HPA
    4. late endosome Source: UniProtKB-SubCell
    5. nucleolus Source: HPA
    6. transport vesicle Source: LIFEdb

    Keywords - Cellular componenti

    Endosome, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 52CC → SS: Loss of association with membranes, no effect on interaction with AP1G1; when associated with 9-S.
    Mutagenesisi9 – 91C → S: Loss of association with membranes, no effect on interaction with AP1G1; when associated with 4-S-S-5. 1 Publication
    Mutagenesisi210 – 2101W → A: Loss of association with the Arp2/3 complex and endosomal colocalization. Abolishes interaction with KLC2, no effect on interaction with AP1G1. 2 Publications
    Mutagenesisi260 – 2601W → L: Decreases interaction with AP1G1; when associated with L-264. 1 Publication
    Mutagenesisi264 – 2641F → L: Decreases interaction with AP1G1; when associated with L-260. 1 Publication

    Organism-specific databases

    PharmGKBiPA165663153.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 302302AP-1 complex-associated regulatory proteinPRO_0000089432Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei228 – 2281Phosphothreonine1 Publication
    Glycosylationi247 – 2471N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Palmitoylated.1 Publication

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ63HQ0.
    PaxDbiQ63HQ0.
    PRIDEiQ63HQ0.

    PTM databases

    PhosphoSiteiQ63HQ0.

    Expressioni

    Gene expression databases

    BgeeiQ63HQ0.
    CleanExiHS_C4orf16.
    GenevestigatoriQ63HQ0.

    Organism-specific databases

    HPAiHPA035863.

    Interactioni

    Subunit structurei

    Interacts (via coiled-coil domain) with AP1G1 (via GAE domain). Interacts with KIF5B. Associates with the Arp2/3 complex.3 Publications

    Protein-protein interaction databases

    BioGridi120667. 2 interactions.
    IntActiQ63HQ0. 1 interaction.
    MINTiMINT-4724276.
    STRINGi9606.ENSP00000274000.

    Structurei

    3D structure databases

    ProteinModelPortaliQ63HQ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni78 – 13861Interaction with AP1G1Add
    BLAST
    Regioni199 – 21517Sufficient for association with the Arp2/3 complexAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili80 – 13859Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi24 – 285Poly-Gly

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG74642.
    HOGENOMiHOG000237335.
    InParanoidiQ63HQ0.
    OMAiSNNGEYQ.
    OrthoDBiEOG7GXPC9.
    PhylomeDBiQ63HQ0.
    TreeFamiTF335676.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q63HQ0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGNCCWTQCF GLLRKEAGRL QRVGGGGGSK YFRTCSRGEH LTIEFENLVE    50
    SDEGESPGSS HRPLTEEEIV DLRERHYDSI AEKQKDLDKK IQKELALQEE 100
    KLRLEEEALY AAQREAARAA KQRKLLEQER QRIVQQYHPS NNGEYQSSGP 150
    EDDFESCLRN MKSQYEVFRS SRLSSDATVL TPNTESSCDL MTKTKSTSGN 200
    DDSTSLDLEW EDEEGMNRML PMRERSKTEE DILRAALKYS NKKTGSNPTS 250
    ASDDSNGLEW ENDFVSAEMD DNGNSEYSGF VNPVLELSDS GIRHSDTDQQ 300
    TR 302
    Length:302
    Mass (Da):34,280
    Last modified:October 25, 2004 - v1
    Checksum:i0827B5EC95DC133A
    GO
    Isoform 2 (identifier: Q63HQ0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         94-126: Missing.

    Show »
    Length:269
    Mass (Da):30,459
    Checksum:i63DCDB9D74E94F2B
    GO

    Sequence cautioni

    The sequence AAF71037.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891K → E in CAB66563. (PubMed:11230166)Curated
    Sequence conflicti217 – 2171N → D in BAG37704. (PubMed:14702039)Curated
    Sequence conflicti243 – 2431K → E in AAH09485. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti297 – 2971T → I.
    Corresponds to variant rs34900583 [ dbSNP | Ensembl ].
    VAR_050769

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei94 – 12633Missing in isoform 2. 1 PublicationVSP_015339Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136628 mRNA. Translation: CAB66563.1.
    BX647702 mRNA. Translation: CAH56145.1.
    AK315299 mRNA. Translation: BAG37704.1.
    AC109347 Genomic DNA. Translation: AAY40962.1.
    BC009485 mRNA. Translation: AAH09485.1.
    AF116612 mRNA. Translation: AAF71037.1. Different initiation.
    CCDSiCCDS3696.1. [Q63HQ0-1]
    CCDS47125.1. [Q63HQ0-2]
    RefSeqiNP_001121898.1. NM_001128426.1. [Q63HQ0-2]
    NP_061039.3. NM_018569.4. [Q63HQ0-1]
    UniGeneiHs.435991.
    Hs.606210.

    Genome annotation databases

    EnsembliENST00000274000; ENSP00000274000; ENSG00000138660. [Q63HQ0-1]
    ENST00000309703; ENSP00000309023; ENSG00000138660. [Q63HQ0-2]
    GeneIDi55435.
    KEGGihsa:55435.
    UCSCiuc003iaj.4. human. [Q63HQ0-1]
    uc003iak.4. human. [Q63HQ0-2]

    Polymorphism databases

    DMDMi73917693.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136628 mRNA. Translation: CAB66563.1 .
    BX647702 mRNA. Translation: CAH56145.1 .
    AK315299 mRNA. Translation: BAG37704.1 .
    AC109347 Genomic DNA. Translation: AAY40962.1 .
    BC009485 mRNA. Translation: AAH09485.1 .
    AF116612 mRNA. Translation: AAF71037.1 . Different initiation.
    CCDSi CCDS3696.1. [Q63HQ0-1 ]
    CCDS47125.1. [Q63HQ0-2 ]
    RefSeqi NP_001121898.1. NM_001128426.1. [Q63HQ0-2 ]
    NP_061039.3. NM_018569.4. [Q63HQ0-1 ]
    UniGenei Hs.435991.
    Hs.606210.

    3D structure databases

    ProteinModelPortali Q63HQ0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120667. 2 interactions.
    IntActi Q63HQ0. 1 interaction.
    MINTi MINT-4724276.
    STRINGi 9606.ENSP00000274000.

    PTM databases

    PhosphoSitei Q63HQ0.

    Polymorphism databases

    DMDMi 73917693.

    Proteomic databases

    MaxQBi Q63HQ0.
    PaxDbi Q63HQ0.
    PRIDEi Q63HQ0.

    Protocols and materials databases

    DNASUi 55435.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274000 ; ENSP00000274000 ; ENSG00000138660 . [Q63HQ0-1 ]
    ENST00000309703 ; ENSP00000309023 ; ENSG00000138660 . [Q63HQ0-2 ]
    GeneIDi 55435.
    KEGGi hsa:55435.
    UCSCi uc003iaj.4. human. [Q63HQ0-1 ]
    uc003iak.4. human. [Q63HQ0-2 ]

    Organism-specific databases

    CTDi 55435.
    GeneCardsi GC04P113153.
    HGNCi HGNC:28808. AP1AR.
    HPAi HPA035863.
    MIMi 610851. gene.
    neXtProti NX_Q63HQ0.
    PharmGKBi PA165663153.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74642.
    HOGENOMi HOG000237335.
    InParanoidi Q63HQ0.
    OMAi SNNGEYQ.
    OrthoDBi EOG7GXPC9.
    PhylomeDBi Q63HQ0.
    TreeFami TF335676.

    Miscellaneous databases

    GeneWikii AP1AR.
    GenomeRNAii 55435.
    NextBioi 35468210.
    PROi Q63HQ0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q63HQ0.
    CleanExi HS_C4orf16.
    Genevestigatori Q63HQ0.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Endometrium and Fetal brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Pancreas.
    5. "Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-302.
      Tissue: Fetal liver.
    6. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    7. "Gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi trafficking."
      Neubrand V.E., Will R.D., Moebius W., Poustka A., Wiemann S., Schu P., Dotti C.G., Pepperkok R., Simpson J.C.
      EMBO J. 24:1122-1133(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AP1G1.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-247.
      Tissue: Leukemic T-cell.
    10. Cited for: FUNCTION, INTERACTION WITH AP1G1; KIF5B AND KLC2, MUTAGENESIS OF TRP-210.
    11. "A novel subtype of AP-1-binding motif within the palmitoylated trans-Golgi network/endosomal accessory protein Gadkin/gamma-BAR."
      Maritzen T., Schmidt M.R., Kukhtina V., Higman V.A., Strauss H., Volkmer R., Oschkinat H., Dotti C.G., Haucke V.
      J. Biol. Chem. 285:4074-4086(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH AP1G1, MUTAGENESIS OF 4-CYS-CYS-5; CYS-9; TRP-260 AND PHE-264.
    12. "Role of AP1 and Gadkin in the traffic of secretory endo-lysosomes."
      Laulagnier K., Schieber N.L., Maritzen T., Haucke V., Parton R.G., Gruenberg J.
      Mol. Biol. Cell 22:2068-2082(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Gadkin negatively regulates cell spreading and motility via sequestration of the actin-nucleating ARP2/3 complex."
      Maritzen T., Zech T., Schmidt M.R., Krause E., Machesky L.M., Haucke V.
      Proc. Natl. Acad. Sci. U.S.A. 109:10382-10387(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-210.

    Entry informationi

    Entry nameiAP1AR_HUMAN
    AccessioniPrimary (citable) accession number: Q63HQ0
    Secondary accession number(s): B2RCV7
    , Q96GG6, Q9H0V0, Q9P1L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3